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Ribosomal RNA Modulates Aggregation of the Podospora Prion Protein HET-s

Yanhong Pang1, Petar Kovachev1, Suparna Sanyal1

  • 1Department of Cell and Molecular Biology, Uppsala University, Box-596, Biomedical Center, 751 24 Uppsala, Sweden.

International Journal of Molecular Sciences
|September 5, 2020
PubMed

Insights

Ribosomal RNA (rRNA) prevents insoluble prion aggregation, promoting soluble seeds for HET-s prion propagation. Domain V of rRNA interacts with HET-s, linking rRNA

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Prion Biology

Background:

  • Nucleic acids play a crucial role in prion aggregation and propagation.
  • The HET-s prion from *Podospora anserina* serves as a model for studying prion behavior.

Purpose of the Study:

  • To investigate the role of ribosomal RNA (rRNA), specifically its domains, in the aggregation and propagation of the HET-s prion.
  • To elucidate the interaction sites between HET-s prion protein and rRNA.

Main Methods:

  • Rayleigh light scattering
  • Thioflavin T (ThT) binding assays
  • Transmission electron microscopy (TEM)
  • Cross-seeding assays
  • Primer extension analysis with UV-crosslinking

Main Results:

  • rRNA, particularly domain V of the large subunit rRNA, significantly inhibits insoluble HET-s prion aggregation in a concentration-dependent manner.
  • rRNA facilitates the formation of soluble oligomeric seeds that promote de novo HET-s prion aggregation.
  • Interaction sites between HET-s and domain V rRNA were identified and overlap with protein-folding activity of the ribosome (PFAR) sites.

Conclusions:

  • Domain V of rRNA plays a critical role in modulating HET-s prion aggregation pathways.
  • This study establishes a link between rRNA-based protein-folding activity and fungal prion propagation mechanisms.
Keywords:
P. anserina prion protein HET-sPFARprion aggregationribosomal RNA

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